Nuclear-inclusion-a endopeptidase

Last updated
Nuclear-inclusion-a endopeptidase
Identifiers
EC no. 3.4.22.44
CAS no. 139946-51-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Nuclear-inclusion-a endopeptidase (EC 3.4.22.44, potyvirus NIa protease) is a protease enzyme found in potyviruses. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction:

Hydrolyses glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus.
e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln \ (Ser or Gly) for the enzyme from tobacco etch virus.

The enzyme is used encoded in vectors for the artificial expression of recombinant fusion proteins (see TEV protease).

Related Research Articles

<span class="mw-page-title-main">Protease</span> Enzyme that cleaves other proteins into smaller peptides

A protease is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds. Proteases are involved in many biological functions, including digestion of ingested proteins, protein catabolism, and cell signaling.

<i>Potyviridae</i> Family of viruses

Potyviridae is a family of positive-strand RNA viruses that encompasses more than 30% of known plant viruses, many of which are of great agricultural significance. The family has 12 genera and 235 species, three of which are unassigned to a genus.

<span class="mw-page-title-main">Cysteine protease</span> Class of enzymes

Cysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad.

<i>Potyvirus</i> Genus of positive-strand RNA viruses in the family Potyviridae

Potyvirus is a genus of positive-strand RNA viruses in the family Potyviridae. Plants serve as natural hosts. Like begomoviruses, members of this genus may cause significant losses in agricultural, pastoral, horticultural, and ornamental crops. More than 200 species of aphids spread potyviruses, and most are from the subfamily Aphidinae. The genus contains 190 species and potyviruses account for about thirty percent of all currently known plant viruses.

<span class="mw-page-title-main">Endopeptidase Clp</span>

Endopeptidase Clp (EC 3.4.21.92, endopeptidase Ti, caseinolytic protease, protease Ti, ATP-dependent Clp protease, ClpP, Clp protease). This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">TEV protease</span> Highly specific protease

TEV protease is a highly sequence-specific cysteine protease from Tobacco Etch Virus (TEV). It is a member of the PA clan of chymotrypsin-like proteases. Due to its high sequence specificity, TEV protease is frequently used for the controlled cleavage of fusion proteins in vitro and in vivo.

Pepper mottle virus (PepMoV) is a plant pathogenic virus in the genus Potyvirus and the virus family Potyviridae. Like other members of the Potyvirus genus, PepMV is a monopartite strand of positive-sense, single-stranded RNA surrounded by a capsid made for a single viral encoded protein. The virus is a filamentous particle that measures about 737 nm in length. Isolates of this virus has been completely sequenced and its RNA is 9640 nucleotides long. This virus is transmitted by several species of aphids in a nonpersitant manner and by mechanical inoculation.

<i>Tobacco etch virus</i> Species of virus

Tobacco etch virus (TEV) is a plant virus in the genus Potyvirus and family Potyviridae. Like other members of the genus Potyvirus, TEV has a monopartite positive-sense, single-stranded RNA genome surrounded by a capsid made from a single viral encoded protein. The virus is a filamentous particle that measures about 730 nm in length. It is transmissible in a non-persistent manner by more than 10 species of aphids including Myzus persicae. It also is easily transmitted by mechanical means but is not known to be transmitted by seeds.

Sweet potato feathery mottle virus (SPFMV) is a member of the genus Potyvirus in the family Potyviridae. It is most widely recognized as one of the most regularly occurring causal agents of sweet potato viral disease (SPVD) and is currently observed in every continent except Antarctica. The number of locations where it is found is still increasing; generally, it is assumed that the virus is present wherever its host is. The virus has four strains that are found in varying parts of the world.

Nepenthesin is an aspartic protease of plant origin that has so far been identified in the pitcher secretions of Nepenthes and in the leaves of Drosera peltata. It is similar to pepsin, but differs in that it also cleaves on either side of Asp residues and at Lys┼Arg. While more pH and temperature stable than porcine pepsin A, it is considerably less stable in urea or guanidine hydrochloride. It is the only known protein with such a stability profile.

Commelina mosaic virus (CoMV) is a plant pathogenic virus in the genus Potyvirus and the virus family Potyviridae. Like other members of the Potyvirus genus, CoMV is a monopartite strand of positive-sense, single-stranded RNA surrounded by a capsid made for a single viral encoded protein. The virus is a filamentous particle that measures about 707-808 nm in length. This virus is transmitted by two species of aphids, Myzus persicae and Aphis gossypii, and by mechanical inoculation.

Passion fruit woodiness virus (PWV) is a plant pathogenic virus in the genus Potyvirus and the virus family Potyviridae. Like other members of the genus Potyvirus, PWV is a monopartite strand of positive-sense, single-stranded RNA surrounded by a capsid made for a single viral encoded protein. The virus is a filamentous particle that measures about 745 nm in length.

Adenain is an enzyme. This enzyme catalyses the following chemical reaction

Helper-component proteinase is an enzyme. This enzyme catalyses the following chemical reaction

V-cath endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">3C-like protease</span> Class of enzymes

The 3C-like protease (3CLpro) or main protease (Mpro), formally known as C30 endopeptidase or 3-chymotrypsin-like protease, is the main protease found in coronaviruses. It cleaves the coronavirus polyprotein at eleven conserved sites. It is a cysteine protease and a member of the PA clan of proteases. It has a cysteine-histidine catalytic dyad at its active site and cleaves a Gln–(Ser/Ala/Gly) peptide bond.

Cassava brown streak virus is a species of positive-strand RNA viruses in the genus Ipomovirus and family Potyviridae which infects plants. Member viruses are unique in their induction of pinwheel, or scroll-shaped inclusion bodies in the cytoplasm of infected cells. Cylindrical inclusion bodies include aggregations of virus-encoded helicase proteins. These inclusion bodies are thought to be sites of viral replication and assembly, making then an important factor in the viral lifecycle. Viruses from both the species Cassava brown streak virus and Ugandan cassava brown streak virus (UCBSV), lead to the development of Cassava Brown Streak Disease (CBSD) within cassava plants.

<span class="mw-page-title-main">Asparagine endopeptidase</span> Class of enzymes

Asparagine endopeptidase is a proteolytic enzyme from C13 peptidase family which hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. It is also known as asparaginyl endopeptidase, citvac, proteinase B, hemoglobinase, PRSC1 gene product or LGMN, vicilin peptidohydrolase and bean endopeptidase. In humans it is encoded by the LGMN gene.

The cardamom mosaic virus (CdMV) is a mosaic virus that affects the production of green cardamom (E. cardamomum). It is a member of the genus Macluravirus (recognized under the family Potyviridae by ICTV in 1988), and is transmitted through aphids (P.caladii) and infected rhizomes, the former in a non-persistent manner.

<i>Onion yellow dwarf virus</i> Species of virus

Onion yellow dwarf virus (OYDV) is a plant virus in the genus Potyvirus that has been identified worldwide and mainly infects species of Allium such as onion, garlic, and leek. The virus causes mild to severe leaf malformation, and bulb reduction up to sixty percent has been observed in garlic.

References

  1. Fellers, J.P.; Collins, G.B.; Hunt, A.G. (1998). "The NIa-proteinase of different plant potyviruses provides specific resistance to viral infection". Crop Sci. 38: 1309–1319. doi:10.2135/cropsci1998.0011183x003800050030x.
  2. Kim, D.-H.; Choi, K.Y. (1998). "Potyvirus NIa protease". In Barrett, A.J.; Rawlings, N.D.; Woessner, J.F. (eds.). Handbook of Proteolytic Enzymes. London: Academic Press. pp. 721–723.
  3. Takahashi T, Nakanishi M, Yao Y, Uyeda I, Serizawa N (May 1998). "Direct formation of human interleukin-11 by cis-acting system of plant virus protease in Escherichia coli". Bioscience, Biotechnology, and Biochemistry. 62 (5): 953–8. doi:10.1271/bbb.62.953. PMID   9648226.
  4. Kim DH, Hwang DC, Kang BH, Lew J, Han J, Song BD, Choi KY (December 1996). "Effects of internal cleavages and mutations in the C-terminal region of NIa protease of turnip mosaic potyvirus on the catalytic activity". Virology. 226 (2): 183–90. doi: 10.1006/viro.1996.0645 . PMID   8955037.